Abstract
THREE different prenyltransferases have been identified in yeast and higher cells1–6, the farnesyltransferase and the type I and type II geranylgeranyltransferases (GGTase). The farnesyltransferase and GGTase-I modify peptides in vitro with the CAAX (C, Cys; A, aliphatic residue; X, terminal amino acid) consensus motif2,7. These enzymes are heterodimers that have different β-subunits and a shared α-subunit8. In yeast, the RAM2 gene encodes this α-subunit9. RAM2 is also homologous to MAD2, a yeast gene whose product has been implicated in the feedback control of mitosis10,11. We have shown that Bet2p is a component of the yeast GGTase-II (refs 6,12) that geranylgeranylates Yptlp, a small GTP-binding protein that mediates transport from the endoplasmic reticulum to the Golgi complex13–15. Here we report that Mad2p is a component of this enzyme. Bet2p forms a complex with Mad2p that appears to bind geranylgeranyl pyrophosphate, but not farnesyl pyrophosphate. The efficient transfer of geranylgeranyl onto small GTP-binding proteins requires the presence of an additional activity.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Reiss, Y., Goldstein, J. L., Seabra, M. C., Casey, P. J. & Brown, M. S. Cell 62, 81–88 (1990).
Moores, S. L. et al. J. biol. Chem. 266, 14603–14610 (1991).
Moomaw, J. F. & Casey, P. J. J. biol. Chem. 267, 17438–17443 (1992).
Schafer, W. R. et al. Science 249, 1133–1139 (1990).
Finegold, A. A. et al. Proc. natn. Acad. Sci. U.S.A. 88, 4448–4452 (1991).
Kohl, N. E. et al. J. biol. Chem. 266, 18884–18888 (1991).
Reiss, Y., Stradley, S. J., Gierasch, L. M., Brown, M. S. & Goldstein, J. L. Proc. natn. Acad. Sci. U.S.A. 88, 732–736 (1991).
Seabra, M. C. Reiss, Y., Casey, P. J., Brown, M. S. & Goldstein, J. L. Cell 65, 429–434 (1991).
He, B. et al. Proc. natn. Acad. Sci. U.S.A. 88, 11373–11377 (1991).
Li, R. & Murray, A. Cell 66, 519–531 (1991).
Boguski, M. S., Murray, A. W. & Powers, S. New Biol. 4, 1–4 (1992).
Rossi, G., Jiang, Y., Newman, A. P. & Ferro-Novick, S. Nature 351, 158–161 (1991).
Segev, N., Mulholland, J. & Botstein, D. Cell 52, 915–924 (1988).
Bacon, R. A., Salminen, A., Ruohola, H., Novick, P. & Ferro-Novick, S. J. Cell Biol. 109, 1015–1022 (1989).
Baker, D., Wuestehube, L., Schekman, R., Botstein, D. & Segev, N. Proc. natn. Acad. Sci. U.S.A. 87, 355–359 (1990).
Salminen, A. & Novick, P. Cell 49, 527–538 (1987).
Seabra, M. C., Goldstein, J., Sudhof, T. C. & Brown, M. S. J. biol. Chem. 267, 14497–14503 (1992).
Seabra, M. C., Brown, M. S., Slaughter, C. A., Sudhof, T. C. & Goldstein, J. L. Cell 70, 1049–1057 (1992).
Kinsella, B. & Maltese, W. A. J. biol. Chem. 266, 8540–8544 (1991).
Mayer, M. L., Caplin, B. E. & Marshall, M. S. J. biol. Chem. 267, 20589–20593 (1992).
Newman, A. & Ferro-Novick, S. J. Cell Biol. 105, 1587–1594 (1987).
Li, R., Havel, C., Watson, J. A. & Murray, A. W. Nature 366, 82–84 (1993).
Andres, D. A. et al. Cell 73, 1091–1099 (1993).
Araki, S., Kikuchi, A., Hata, Y., Isomura, M. & Takai, Y. J. biol. Chem. 265, 13007–13015 (1990).
Armstrong, S. A., Seabra, M. C., Sudhof, T. C., Goldstein, J. L. & Brown, M. S. J. biol. Chem. 268, 12221–12229 (1993).
Wagner, P. et al. EMBO J. 6, 2373–2379 (1987).
Walworth, N. C., Brennwald, P., Kabcenell, A. K., Garrett, M. & Novick, P. Molec. cell. Biol. 12, 2017–2028 (1992).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Jiang, Y., Rossi, G. & Ferro-Novick, S. Bet2p and Mad2p are components of a prenyltransferase that adds geranylgeranyl onto Ypt1p and Sec4p. Nature 366, 84–86 (1993). https://doi.org/10.1038/366084a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/366084a0
This article is cited by
-
Identifying cross-category relations in gene ontology and constructing genome-specific term association networks
BMC Bioinformatics (2013)
-
The yeast protein Mrs6p, a homologue of the rabGDI and human choroideraemia proteins, affects cytoplasmic and mitochondrial functions
Current Genetics (1994)
-
Mrs6p, the yeast homologue of the mammalian choroideraemia protein: immunological evidence for its function as the Ypt1p Rab escort protein
Current Genetics (1994)
-
Mad Bet for Rab
Nature (1993)
-
The mitotic feedback control gene MAD2 encodes the α-subunit of a prenyltransferase
Nature (1993)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
